Cited by 641Heat shock proteins researchFungal and yeast genetics researchUbiquitin and proteasome pathways

The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Open access

Borkovich, K A, Farrelly, F W, Finkelstein, D B, Taulien, J, Lindquist, S·1989·Molecular and Cellular Biology

Open this paper in CoChat — free account

Abstract

hsp82 is one of the most highly conserved and abundantly synthesized heat shock proteins of eucaryotic cells. The yeast Saccharomyces cerevisiae contains two closely related genes in the HSP82 gene family. HSC82 was expressed constitutively at a very high level and was moderately induced by high temperatures. HSP82 was expressed constitutively at a much lower level and was more strongly induced by heat. Site-directed disruption mutations were produced in both genes. Cells homozygous for both mutations did not grow at any temperature. Cells carrying other combinations of the HSP82 and HSC82 mutations grew well at 25 degrees C, but their ability to grow at higher temperatures varied with gene copy number. Thus, HSP82 and HSC82 constitute an essential gene family in yeast cells. Although the two proteins had different patterns of expression, they appeared to have equivalent functions; growth at higher temperatures required higher concentrations of either protein. Biochemical analysis of hsp82 from vertebrate cells suggests that the protein binds to a variety of other cellular proteins, keeping them inactive until they have reached their proper intracellular location or have received the proper activation signal. We speculate that the reason cells require higher concentrations of hsp82 or hsc82 for growth at higher temperatures is to maintain proper levels of complex formation with these other proteins.

Integrity signals

Registry

Crossref · 10.1128/mcb.9.9.3919

Cites

58 of 58 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

The text we found for this paper looks like another document, so its claims and self-check weren’t run. The registry and citation checks still apply.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The text we found for this paper looks like another document, so the self-check wasn’t run.

Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular Cloning. A Laboratory Manual
Wood, E. (1983) · Biochemical Education · doi:10.1016/0307-4412(83)90068-7 · Cited by 29,534
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222
Transformation of intact yeast cells treated with alkali cations
Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518
THE HEAT-SHOCK PROTEINS
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304
Self-citation
[12] One-step gene disruption in yeast
Rothstein, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)01015-0 · Cited by 3,282
High-frequency transformation of yeast: autonomous replication of hybrid DNA molecules.
Struhl, K., Stinchcomb, D. T., Scherer, S., & Davis, R. W. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.3.1035 · Cited by 1,456
Transformation in yeast: Development of a hybrid cloning vector and isolation of the can1 gene
Broach, J. R., Strathern, J. N., & Hicks, J. B. (1979) · Gene · doi:10.1016/0378-1119(79)90012-x · Cited by 1,073
Principles of protein–protein recognition
Chothia, C., & Janin, J. (1975) · Nature · doi:10.1038/256705a0 · Cited by 1,049
A regulatory upstream promoter element in the Drosophila Hsp 70 heat-shock gene
Pelham, H. R. B. (1982) · Cell · doi:10.1016/0092-8674(82)90249-5 · Cited by 973
The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
Finley, D., Özkaynak, E., & Varshavsky, A. J. (1987) · Cell · doi:10.1016/0092-8674(87)90711-2 · Cited by 860
The htpR gene product of E. coli is a sigma factor for heat-shock promoters
Grossman, A. D., Erickson, J. W., & Gross, C. A. (1984) · Cell · doi:10.1016/0092-8674(84)90493-8 · Cited by 592
Key features of heat shock regulatory elements.
Αmin, J., Ananthan, J., & Voellmy, R. W. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3761 · Cited by 572
[49] Rapid DNA isolations for enzymatic and hybridization analysis
Davis, R. W., Thomas, M., Cameron, J., John, T. P. S., Scherer, S., & Padgett, R. A. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(80)65051-4 · Cited by 555
Germline Transformation Used to Define Key Features of Heat-Shock Response Elements
Xiao, H., & Lis, J. T. (1988) · Science · doi:10.1126/science.3125608 · Cited by 455
The structure of transposable yeast mating type loci
Nasmyth, K., & Tatchell, K. (1980) · Cell · doi:10.1016/s0092-8674(80)80051-1 · Cited by 437
Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones
Joab, I., Radanyi, C., Renoir, M., Buchou, T., CATELLI, M. G., Binart, N., Mešter, J., & Baulieu, É.-É. (1984) · Nature · doi:10.1038/308850a0 · Cited by 434
The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins
Brugge, J. S., ERIKSON, E., & Erikson, R. L. (1981) · Cell · doi:10.1016/0092-8674(81)90055-6 · Cited by 336
Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.
Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K., Harada, F., Kasuga, M., Sakai, H., & Yahara, I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8054 · Cited by 329
ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).
Mazzarella, R. A., & Green, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47496-0 · Cited by 289
Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth
Craig, E. A., & Jacobsen, K. (1984) · Cell · doi:10.1016/0092-8674(84)90279-4 · Cited by 286
Activation of heat-shock genes in eukaryotes
Pelham, H. R. B. (1985) · Trends in Genetics · doi:10.1016/0168-9525(85)90012-5 · Cited by 265
Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor.
Sánchez, E. R., Meshinchi, S., Tienrungroj, W., Schlesinger, M. J., Toft, D. O., & Pratt, W. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48191-4 · Cited by 263
Hsp26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germination
Petko, L., & Lindquist, S. L. (1986) · Cell · doi:10.1016/0092-8674(86)90563-5 · Cited by 231
Self-citation
Interspecific nucleotide sequence comparisons used to identify regulatory and structural features of the Drosophila hsp82 gene
Blackman, R. K., & Meselson, M. S. (1986) · Journal of Molecular Biology · doi:10.1016/s0022-2836(86)80001-8 · Cited by 223
Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.
Bardwell, J. C. A., & Craig, E. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5177 · Cited by 212
SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth.
Craig, E. A., Kramer, J., & Kosic-Smithers, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.12.4156 · Cited by 202
Key Features of Heat Shock Regulatory Elements
Αmin, J., Ananthan, J., & Voellmy, R. W. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3761-3769.1988 · Cited by 197
Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae.
Farrelly, F. W., & FINKELSTEIN, D. B. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91077-x · Cited by 188
Self-citation
Polypeptide components of two 8 S forms of chicken oviduct progesterone receptor.
Dougherty, J. J., Puri, R. K., & Toft, D. O. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42893-6 · Cited by 186
Ancient heat shock gene is dispensable
Bardwell, J. C. A., & Craig, E. A. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.7.2977-2983.1988 · Cited by 181
Induction of the heat shock regulon does not produce thermotolerance in Escherichia coli.Preprint
VanBogelen, R. A., Acton, M., & Neidhardt, F. C. (1987) · Genes & Development · doi:10.1101/gad.1.6.525 · Cited by 177
Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein.
Buss, J. E., Kamps, M. P., & Sefton, B. M. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.12.2697 · Cited by 172
Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family
Rebbe, N. F., Ware, J. L., Bertina, R. M., Modrich, P. L., & Stafford, D. W. (1987) · Gene · doi:10.1016/0378-1119(87)90012-6 · Cited by 166
Transit of pp60v-src to the plasma membrane.
Courtneidge, S. A., & Bishop, J. M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.23.7117 · Cited by 165
Calmodulin-regulated binding of the 90-kDa heat shock protein to actin filaments.
Nishida, E., Koyasu, S., Sakai, H., & Yahara, I. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66671-2 · Cited by 158
Interaction Between the Rous Sarcoma Virus Transforming Protein and Two Cellular Phosphoproteins: Analysis of the Turnover and Distribution of This Complex
Brugge, J. S., Yonemoto, W. M., & Darrow, D. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.1.9-19.1983 · Cited by 158
The Genome of Trypanosoma cruzi Contains a Constitutively Expressed, Tandemly Arranged Multicopy Gene Homologous to a Major Heat Shock Protein
Dragon, E. A., Sias, S. R., KATO, E. A., & Gabe, J. D. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.3.1271-1275.1987 · Cited by 132
Transcriptional regulation of an hsp70 heat shock gene in the yeast Saccharomyces cerevisiae.
Slater, M. R., & Craig, E. A. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.5.1906 · Cited by 128
Molecular cloning and expression of a gene that controls the high-temperature regulon of Escherichia coli
Neidhardt, F. C., VanBogelen, R. A., & Lau, E. T. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.2.597-603.1983 · Cited by 127
The 90-kilodalton peptide of the heme-regulated eIF-2.alpha. kinase has sequence homology with the 90-kilodalton heat shock protein
Rose, D. W., Wettenhall, R. E. H., Kudlicki, W. A., Kramer, G., & Hardesty, B. (1987) · Biochemistry · doi:10.1021/bi00395a003 · Cited by 126
Association of the transforming proteins of Rous, Fujinami, and Y73 avian sarcoma viruses with the same two cellular proteins.
Lipsich, L. A., Cutt, J. R., & Brugge, J. S. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.7.875 · Cited by 117
Changing patterns of gene expression during sporulation in yeast.
Kurtz, S. E., & Lindquist, S. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.23.7323 · Cited by 117
Self-citation
Evidence that the 90-Kilodalton Heat Shock Protein is Associated with Tubulin-Containing Complexes in L Cell Cytosol and in Intact PtK Cells
Sánchez, E. R., Redmond, T., Scherrer, L. C., Bresnick, E. H., Welsh, M. J., & Pratt, W. B. (1988) · Molecular Endocrinology · doi:10.1210/mend-2-8-756 · Cited by 113
Subunit composition of the molybdate-stabilized “8-9 S” nontransformed estradiol receptor purified from calf uterus.
Redeuilh, G., Moncharmont, B., Secco, C., & Baulieu, E. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48188-4 · Cited by 111
Effects of Cycloheximide on Thermotolerance Expression, Heat Shock Protein Synthesis, and Heat Shock Protein mRNA Accumulation in Rat Fibroblasts
Widelitz, R. B., Magun, B. E., & Gerner, E. W. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.4.1088 · Cited by 100
Thermotolerance in Mammalian Cells: A Possible Role for Heat Shock Proteins
Li, G. C., & Laszlo, A. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-066290-6.50017-6 · Cited by 98
Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex.
Brugge, J. S., Yonemoto, W. M., & Darrow, D. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.1.9 · Cited by 89
Mitochondrial and cytoplasmic protein syntheses are not required for heat shock acquisition of ethanol and thermotolerance in yeast
Watson, K., Dunlop, G., & Cavicchioli, R. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)81145-x · Cited by 71
Involvement of a non-hormone-binding 90-kilodalton protein in the nontransformed 8S form of the rabbit uterus progesterone receptor
Renoir, J. M., Buchou, T., & Baulieu, E. E. (1986) · Biochemistry · doi:10.1021/bi00369a010 · Cited by 63
Thermotolerance induced by heat, sodium arsenite, or puromycin: Its inhibition and differences between 43°C and 45°C
Lee, Y. J., & Dewey, W. C. (1988) · Journal of Cellular Physiology · doi:10.1002/jcp.1041350306 · Cited by 59
Heat shock causes diverse changes in the phosphorylation of the ribosomal proteins of mammalian cells
Kennedy, I. M., Burdon, R. H., & Leader, D. P. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80331-2 · Cited by 54
Transcriptional Regulation of an hsp70 Heat Shock Gene in the Yeast Saccharomyces Cerevisiae
Slater, M. R., & Craig, E. A. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.5.1906-1916.1987 · Cited by 54
The molybdate-stabilized glucocorticoid binding complex of L-cells contains a 98–100 kdalton steroid binding phosphoprotein and a 90 kdalton nonsteroid-binding phosphoprotein that is part of the murine heat-shock complex
Sánchez, E. R., Housley, P. R., & Pratt, W. B. (1986) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(86)90025-7 · Cited by 52
Purification and characterization of arginase from Neurospora crassa.
Borkovich, K. A., & Weiss, R. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48206-3 · Cited by 50
Self-citation
The transforming proteins of PRCII virus and Rous sarcoma virus form a complex with the same two cellular phosphoproteins
Adkins, B., Hunter, T. R., & Sefton, B. M. (1982) · Journal of Virology · doi:10.1128/jvi.43.2.448-455.1982 · Cited by 49
Association of the Transforming Proteins of Rous, Fujinami, and Y73 Avian Sarcoma Viruses with the Same Two Cellular Proteins
Lipsich, L. A., Cutt, J. R., & Brugge, J. S. (1982) · Molecular and Cellular Biology · doi:10.1128/mcb.2.7.875-880.1982 · Cited by 37
Characterization of the monomeric and complex-associated forms of the gag-onc fusion proteins of three isolates of feline sarcoma virus: Phosphorylation, kinase activity, acylation, and kinetics of complex formation
Ziemiecki, A. (1986) · Virology · doi:10.1016/0042-6822(86)90048-6 · Cited by 18

Sorted by citations

THE FUNCTION OF HEAT-SHOCK PROTEINS IN STRESS TOLERANCE: DEGRADATION AND REACTIVATION OF DAMAGED PROTEINS
Parsell, D. A., & Lindquist, S. (1993) · Annual Review of Genetics · doi:10.1146/annurev.ge.27.120193.002253 · Cited by 2,275
Self-citation
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Self-citation
The HSP90 chaperone machinery
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
Remodeling of Yeast Genome Expression in Response to Environmental Changes
Causton, H. C., Ren, B., Koh, S. S., Harbison, C. T., Kanin, E. I., Jennings, E. G., Lee, T. I., True, H. L., Lander, E. S., & Young, R. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.2.323 · Cited by 1,382
Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370

See all 641

Authors: Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Borkovich, K A
Finkelstein, D B
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 1989-09
Volume: 9
Issue: 9
Pages: 3919-3930
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.9.9.3919
PMC: PMC362454
OpenAlex: W1956379070
Cited by: 641
References: 54
Citations by year: 2026: 1 · 2025: 5 · 2024: 22 · 2023: 11 · 2022: 19 · 2021: 16 · 2020: 15 · 2019: 23 · 2018: 16 · 2017: 16 · 2016: 18 · 2015: 11 · 2014: 32 · 2013: 26 · 2012: 24
FWCI: 5.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Molecular and Cellular Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM 11223, GM3582, GM25829)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: Hsp82, heat shock proteins, Saccharomyces cerevisiae, heat tolerance, gene copy number, site-directed mutagenesis, protein-protein complex formation, molecular chaperones, constitutive expression
MeSH terms: Amino Acid Sequence, Base Sequence, DNA, Fungal, Gene Expression Regulation, Genes, Fungal, Multigene Family, Hot Temperature, Heat-Shock Proteins, Molecular Sequence Data, Mutation, Saccharomyces cerevisiae, Spores, Fungal

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks